JPH09511914A - ペスチウイルス株のヌクレオチド配列、それらの配列によりコードされるポリペプチド、ならびにペスチウイルス感染の診断および予防のためのそれらの使用 - Google Patents
ペスチウイルス株のヌクレオチド配列、それらの配列によりコードされるポリペプチド、ならびにペスチウイルス感染の診断および予防のためのそれらの使用Info
- Publication number
- JPH09511914A JPH09511914A JP8501973A JP50197396A JPH09511914A JP H09511914 A JPH09511914 A JP H09511914A JP 8501973 A JP8501973 A JP 8501973A JP 50197396 A JP50197396 A JP 50197396A JP H09511914 A JPH09511914 A JP H09511914A
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- JP
- Japan
- Prior art keywords
- nucleotide sequence
- strain
- sequence
- pestivirus
- csfv
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
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- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
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- A61P31/12—Antivirals
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
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- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2770/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses positive-sense
- C12N2770/00011—Details
- C12N2770/24011—Flaviviridae
- C12N2770/24311—Pestivirus, e.g. bovine viral diarrhea virus
- C12N2770/24322—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
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Abstract
Description
Claims (1)
- 【特許請求の範囲】 1.古典的ブタコレラウイルス(CSFV)のゲノム、またはその一部分もし くは突然変異体に相当し、配列番号1に示されるCSFV C−株のヌクレオチ ド配列、またはそのようなヌクレオチド配列の相補物もしくはRNA相同物の少 なくとも一部分を含むことを特徴とするヌクレオチド配列。 2.古典的ブタコレラウイルス(CSFV)のゲノム、またはその一部分もし くは突然変異体に相当し、配列番号1に示されるアミノ酸配列の内の少なくとも アミノ酸配列268−494をコードするヌクレオチド配列、またはそのような ヌクレオチド配列の相補物もしくはRNA相同物を含むことを特徴とするヌクレ オチド配列。 3.配列番号1に示される配列の内のアミノ酸配列1−1063をコードする ヌクレオチド配列内に一つの突然変異を含む、請求の範囲1もしくは2に記載の ヌクレオチド配列。 4.アミノ酸690−870をコードするヌクレオチド配列内に一つの突然変 異を含む、請求の範囲3に記載のヌクレオチド配列。 5.前記突然変異が、他のペスチウイルス株のゲノムの対応部分による置換で ある、請求の範囲1〜4の内のいずれか一つに記載のヌクオチド配列。 6.前記突然変異が、欠失、挿入、またはそのヌクレオチド配列によりコード される一つもしくは複数のアミノ酸の置換をもたらす突然変異である、請求の範 囲1〜4の内のいずれか一つに記載のヌクレオチド配列。 7.前記突然変異が、CSFVヌクレオチド配列の翻訳方法を変化さ せるか、あるいはCSFVヌクレオチド配列によりコードされるポリペプチドの プロセシングを変化させる異種ヌクレオチド配列の挿入である、請求の範囲1〜 4の内のいずれか一つに記載のヌクレオチド配列。8.前記突然変異が、他の病 原体に対する免疫を誘導するポリペプチドをコードする異種ヌクレオチド配列の 挿入である、請求の範囲1〜4の内のいずれか一つに記載のヌクレオチド配列。 9.前記突然変異が、マーカーポリペプチドをコードする異種ヌクレオチド配 列の挿入である、請求の範囲1〜4の内のいずれか一つに記載のヌクレオチド配 列。 10.請求の範囲1〜9の内のいずれか一つに記載のヌクレオチド配列によりコ ードされるポリペプチド。 11.配列番号1のアミノ酸配列690−1063もしくはその部分に相当し、 アミノ酸配列691−750もしくは785−870内に含まれるエピトープの 内の一つに一つの突然変異を含み、前記突然変異が前記エピトープを変化させる ことを特徴とする、ペスチウイルスのポリペプチド。 12.請求の範囲11に記載のポリペプチドをコードするヌクレオチド配列。 13.そのゲノムが、請求の範囲1〜8の内のいずれか一つに記載のヌクレオチ ド配列の全長DNAコピーおよび/またはその感染性転写物に由来するワクチン 株。 14.請求の範囲1〜9もしくは12の内のいずれか一つに記載の配列を有する ポリヌクレオチド、請求の範囲10もしくは11に記載のポリペプチド、または 請求の範囲13に記載のワクチン株を含むワクチン。 15.請求の範囲1〜9の内のいずれか一つに記載のヌクレオチド配列、請求の 範囲10もしくは11に記載のポリペプチド、および/または請求の範囲10も しくは11に記載のポリペプチドに対して作製された抗体を少なくとも含む、診 断用組成物。 16.CSFV C−株由来の配列のためのマーカーとしての、ヌクレオチド配 列TTTTCTTTTTTTTの使用。 17.予防接種を施した動物からペスチウイルスに感染した動物を識別し、前記 予防接種を施した動物が、配列番号1のアミノ酸配列268−494もしくは6 90−1063に一つの突然変異を含むペスチウイルスポリペプチドもしくはペ スチウイルス株での予防接種を施され、ある検査用試料を、アミノ酸配列268 −494もしくはアミノ酸配列690−1063に相当するペスチウイルス抗原 またはそれらの部分、および前記ペスチウイルス抗原のエピトープに対して作製 された抗体と接触させ、そのエピトープは予防接種に用いられる突然変異を生じ させたポリペプチドもしくはペスチウイルス株内に機能的状態では存在しない、 診断方法。 18.前記ペスチウイルス抗原が二量体もしくは多量体を形成するポリペプチド であって、かつ前記抗体の部分が固定化されており、そして前記抗体の他の部分 がラベル化されている、請求の範囲17に記載の方法。 19.前記ペスチウイルスポリペプチドおよび前記抗原がアミノ酸配列690− 1063に相当し、そして前記エピトープがアミノ酸785と870との間に位 置する、請求の範囲17もしくは18に記載の方法。 20.ある試料中で、ある結合相手の結合部位に特異的に結合することが可能な 検査用物質の存在を、前記検査用物質と、前記結合相手の同一 の結合部位と特異的に結合することが可能な対照用物質の測定可能量との競合に より決定する: (1)前記試料を、(a)前記対照用物質の結合相手(前記結合相手分子は、前 記対照用物質のための少なくとも2つの同一な結合部位を含む)、(b)固体担 体に結合させてある前記対照用物質、および(c)ラベルが提供されている前記 対照用物質、と接触させること; (2)前記担体への前記ラベルの結合の度合いを測定すること、 を含む方法。 21.前記結合相手が、前記対照用物質に対する結合相手の二量体もしくは多量 体である、請求の範囲20に記載の方法。 22.ある試料中で、ある結合相手との特異的に結合について、分子当たり少な くとも2つの同一な結合部位を有する検査用物質の存在を決定する: (1)前記試料を、(a)固体担体に結合させてある前記結合相手、および(b )ラベルが提供されている前記結合相手物質、と接触させること; (2)前記担体への前記ラベルの結合の度合いを測定すること、 を含む方法。 23.(a)固体担体に結合させてある対照用抗体、(b)ラベルが提供されて 入る前記対照用抗体;および場合によっては(c)前記対照用抗体のための少な くとも2つの同一な結合部位を含む、前記対照用抗体に対する抗原か;あるいは 前記構成成分(a)、(b)、および(c)の間の複合体;ならびに競合的免疫 学的アッセイを実施するための更に別の構成成分、を含む診断用キット。
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EP94201743.5 | 1994-06-17 | ||
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PCT/NL1995/000214 WO1995035380A1 (en) | 1994-06-17 | 1995-06-16 | Nucleotide sequences of pestivirus strains, polypeptides encoded by these sequences and use thereof for diagnosis and prevention of pestivirus infections |
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JPH09511914A true JPH09511914A (ja) | 1997-12-02 |
JP3846808B2 JP3846808B2 (ja) | 2006-11-15 |
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US (1) | US6180109B1 (ja) |
EP (2) | EP1985705A3 (ja) |
JP (1) | JP3846808B2 (ja) |
CN (2) | CN101255433A (ja) |
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BR (1) | BR9508054A (ja) |
CA (1) | CA2192940C (ja) |
CZ (1) | CZ295138B6 (ja) |
HU (1) | HU220746B1 (ja) |
MX (1) | MX9606463A (ja) |
NZ (1) | NZ287563A (ja) |
PL (1) | PL184836B1 (ja) |
RU (1) | RU2201451C2 (ja) |
WO (1) | WO1995035380A1 (ja) |
ZA (1) | ZA955042B (ja) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2005509399A (ja) * | 2000-11-14 | 2005-04-14 | モーフオテク・インコーポレーテツド | 遺伝的に改変された抗原の生成法 |
Families Citing this family (20)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EP0924298A1 (en) * | 1997-12-18 | 1999-06-23 | Stichting Instituut voor Dierhouderij en Diergezondheid (ID-DLO) | Protein expression in baculovirus vector expression systems |
EP0982402A1 (en) * | 1998-08-14 | 2000-03-01 | Stichting Instituut voor Dierhouderij en Diergezondheid (ID-DLO) | Pestivirus vaccination |
CN1338309A (zh) * | 2000-08-10 | 2002-03-06 | 清华大学 | 一种合成肽猪瘟疫苗及其制备方法 |
CN1338310A (zh) * | 2000-08-10 | 2002-03-06 | 清华大学 | 一种猪瘟病毒表位疫苗及其制备方法 |
US6686432B2 (en) * | 2002-02-15 | 2004-02-03 | Ppg Industries Ohio, Inc. | Alternating copolymers of isobutylene type monomers |
WO2004016794A1 (en) * | 2002-08-13 | 2004-02-26 | Akzo Nobel N.V. | Replicons of pestiviruses that do not express c and or e1 protein and infectious viral particles containing same, that can be used in vaccines |
ES2390874T3 (es) * | 2002-11-08 | 2012-11-19 | The Administrators Of The Tulane Educational Fund | Inhibidores de fusión de flavivirus |
AU2007242061B2 (en) | 2006-04-21 | 2012-11-29 | Intervet International B.V. | Pestivirus species |
AU2013200106B2 (en) * | 2006-04-21 | 2015-10-01 | Intervet International Bv | Pestivirus Species |
US9359411B2 (en) * | 2008-07-31 | 2016-06-07 | Maw Hsing Biotech Co., Ltd. | Yeast expressed classical swine fever virus glycoprotein E2 and use thereof |
US20100104597A1 (en) * | 2008-10-24 | 2010-04-29 | Manuel Borca | N-linked glycosylation alteration in E0 and E2 glycoprotein of classical swine fever virus and novel classical swine fever virus vaccine |
EP2202298A1 (en) | 2008-12-23 | 2010-06-30 | Stichting Dienst Landbouwkundig Onderzoek | Recombinant classical swine fever virus (CSFV) comprising a modified E2 protein and methods for generating said recombinant CSFV |
US8063195B2 (en) * | 2009-05-22 | 2011-11-22 | The United States Of America As Represented By The Secretary Of Agriculture | Mutations in a toll-like receptor motif in the NS4B of classical swine fever virus strain brescia influences virulence in swine |
EA031518B1 (ru) * | 2010-05-18 | 2019-01-31 | Римзер Фарма Гмбх | Маркерная вакцина против классической чумы свиней |
BR112016014010B1 (pt) * | 2013-12-19 | 2022-08-30 | Intervet International B.V. | Método para detectar anticorpos contra vírus da febre suína clássica tipo selvagem (csfv) em uma amostra de teste e kit de teste de diagnóstico |
KR101886286B1 (ko) * | 2016-11-21 | 2018-08-10 | 주식회사 옵티팜 | 돼지파보바이러스 및 돼지열병바이러스에 대한 동시 항원성 복합 항원 단백질의 제조 방법 |
CN108315306B (zh) * | 2018-01-05 | 2020-06-16 | 浙江大学 | 一株高繁殖能力猪瘟病毒及其构建方法 |
CN108530532B (zh) * | 2018-04-13 | 2021-04-27 | 吉林大学 | 猪瘟病毒单克隆抗体hk 44及医用用途 |
CN111575404B (zh) * | 2020-05-08 | 2023-03-14 | 中国兽医药品监察所 | 对猪瘟野毒及其疫苗、非洲猪瘟病毒进行鉴别诊断的基因芯片以及检测方法 |
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---|---|---|---|---|
ZA864879B (en) | 1985-07-08 | 1987-03-25 | Wallone Region | Vaccines and diagnostics derived from boving diarrhoea virus |
EP0231209B1 (en) * | 1985-07-29 | 1991-02-06 | The Upjohn Company | Virus vaccine |
US4753884A (en) * | 1986-01-28 | 1988-06-28 | Novagene, Inc. | Pseudorabies virus mutants, vaccines containing same, methods for the production of same and methods for the use of same |
NL8703107A (nl) * | 1987-12-22 | 1989-07-17 | Nederlanden Staat | Polypeptiden en derivaten daarvan, alsmede de toepassing daarvan in farmaceutische en diagnostische preparaten. |
NL8801601A (nl) * | 1988-06-23 | 1990-01-16 | Centraal Diergeneeskundig Inst | Een "swine-kidney" celcultuur, geschikt voor het kweken van virussen, een daaraan geadapteerde "chinese" stam van het varkenspestvirus, alsmede de hiervan afgeleide vaccins. |
US5122447A (en) | 1989-01-23 | 1992-06-16 | Iowa State University Research Foundation, Inc. | Method of detecting pseudorabies virus specific serum antibody by use of a universal diagnostic antigen |
NL8901651A (nl) * | 1989-06-29 | 1991-01-16 | Centraal Diergeneeskundig Inst | Vaccin tegen pestivirusinfecties, zoals varkenspest; daarvoor bruikbare nucleotidesequenties en polypeptiden. |
-
1995
- 1995-06-16 CA CA002192940A patent/CA2192940C/en not_active Expired - Fee Related
- 1995-06-16 EP EP08151123A patent/EP1985705A3/en not_active Withdrawn
- 1995-06-16 RU RU97100934/13A patent/RU2201451C2/ru not_active IP Right Cessation
- 1995-06-16 US US08/750,717 patent/US6180109B1/en not_active Expired - Fee Related
- 1995-06-16 MX MX9606463A patent/MX9606463A/es not_active IP Right Cessation
- 1995-06-16 WO PCT/NL1995/000214 patent/WO1995035380A1/en active IP Right Grant
- 1995-06-16 CZ CZ19963696A patent/CZ295138B6/cs not_active IP Right Cessation
- 1995-06-16 JP JP50197396A patent/JP3846808B2/ja not_active Expired - Fee Related
- 1995-06-16 BR BR9508054A patent/BR9508054A/pt not_active Application Discontinuation
- 1995-06-16 PL PL95317755A patent/PL184836B1/pl not_active IP Right Cessation
- 1995-06-16 AU AU26315/95A patent/AU697866B2/en not_active Ceased
- 1995-06-16 NZ NZ287563A patent/NZ287563A/en not_active IP Right Cessation
- 1995-06-16 HU HU9603470A patent/HU220746B1/hu not_active IP Right Cessation
- 1995-06-16 CN CNA200710169874XA patent/CN101255433A/zh active Pending
- 1995-06-16 EP EP95921167A patent/EP0766740A1/en not_active Withdrawn
- 1995-06-16 CN CNB951936654A patent/CN100516221C/zh not_active Expired - Fee Related
- 1995-06-19 ZA ZA955042A patent/ZA955042B/xx unknown
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2005509399A (ja) * | 2000-11-14 | 2005-04-14 | モーフオテク・インコーポレーテツド | 遺伝的に改変された抗原の生成法 |
Also Published As
Publication number | Publication date |
---|---|
CZ369696A3 (en) | 1997-06-11 |
AU2631595A (en) | 1996-01-15 |
HUT76352A (en) | 1997-08-28 |
CA2192940A1 (en) | 1995-12-28 |
EP1985705A3 (en) | 2008-12-10 |
AU697866B2 (en) | 1998-10-22 |
US6180109B1 (en) | 2001-01-30 |
PL184836B1 (pl) | 2002-12-31 |
BR9508054A (pt) | 1997-08-12 |
EP1985705A2 (en) | 2008-10-29 |
PL317755A1 (en) | 1997-04-28 |
CN101255433A (zh) | 2008-09-03 |
NZ287563A (en) | 1998-08-26 |
JP3846808B2 (ja) | 2006-11-15 |
CA2192940C (en) | 2009-08-11 |
MX9606463A (es) | 1997-12-31 |
RU2201451C2 (ru) | 2003-03-27 |
EP0766740A1 (en) | 1997-04-09 |
WO1995035380A1 (en) | 1995-12-28 |
HU220746B1 (hu) | 2002-05-28 |
CN100516221C (zh) | 2009-07-22 |
ZA955042B (en) | 1996-02-08 |
CZ295138B6 (cs) | 2005-05-18 |
CN1151185A (zh) | 1997-06-04 |
HU9603470D0 (en) | 1997-02-28 |
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